Protein Tyrosine Phosphatases (PTPs) are a group of enzymes that play a crucial role in regulating cellular processes by dephosphorylating tyrosine residues on proteins. Among these, Protein Tyrosine Phosphatase Non-Receptor Type-4 (PTPN4) is a significant member that has garnered attention due to its involvement in various cellular functions and disease mechanisms.
PTPN4 is characterized by its structure, which includes a C-terminal PTP domain and an N-terminal domain homologous to the band 4.1 superfamily of cytoskeletal-associated proteins . This structural composition allows PTPN4 to interact with various cellular components and participate in signaling pathways.
The primary function of PTPN4 is to dephosphorylate receptor protein tyrosine kinases such as INSR, EGFR, CSF1R, and PDGFR, as well as non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, and Src family kinases . This dephosphorylation activity is crucial for regulating cell growth, differentiation, mitotic cycle, and oncogenic transformation.
PTPN4 is involved in several cellular processes, including:
The expression patterns of PTPN4 and other PTPN family members have been studied extensively in various cancers, including digestive tract cancers . Alterations in PTPN4 expression are associated with the incidence, prognosis, and pathological grade of these cancers. For instance, high expression levels of PTPN4 have been observed in esophageal and gastric cancer cell lines .
Research on PTPN4 continues to uncover its potential as a therapeutic target. By understanding the molecular mechanisms regulated by PTPN4, scientists aim to develop targeted therapies for diseases associated with its dysregulation. The recombinant form of human PTPN4 is used in research to study its function and to screen for potential inhibitors that could be used in cancer treatment.